View source for 6qdj


==Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin==
<StructureSection load='6qdj' size='340' side='right'caption='[[6qdj]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qdj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QDJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.884&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=P15:2,5,8,11,14,17-HEXAOXANONADECAN-19-OL'>P15</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qdj OCA], [https://pdbe.org/6qdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qdj RCSB], [https://www.ebi.ac.uk/pdbsum/6qdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qdj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYO4_CAEEL MYO4_CAEEL] Required for muscle contraction.<ref>PMID:27123983</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Myosin is a motor protein that is essential for a variety of processes ranging from intracellular transport to muscle contraction. Folding and assembly of myosin relies on a specific chaperone, UNC-45. To address its substrate-targeting mechanism, we reconstitute the interplay between Caenorhabditis elegans UNC-45 and muscle myosin MHC-B in insect cells. In addition to providing a cellular chaperone assay, the established system enabled us to produce large amounts of functional muscle myosin, as evidenced by a biochemical and structural characterization, and to directly monitor substrate binding to UNC-45. Data from in vitro and cellular chaperone assays, together with crystal structures of binding-deficient UNC-45 mutants, highlight the importance of utilizing a flexible myosin-binding domain. This so-called UCS domain can adopt discrete conformations to efficiently bind and fold substrate. Moreover, our data uncover the molecular basis of temperature-sensitive UNC-45 mutations underlying one of the most prominent motility defects in C. elegans.

Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.,Hellerschmied D, Lehner A, Franicevic N, Arnese R, Johnson C, Vogel A, Meinhart A, Kurzbauer R, Deszcz L, Gazda L, Geeves M, Clausen T Nat Commun. 2019 Oct 21;10(1):4781. doi: 10.1038/s41467-019-12667-8. PMID:31636255<ref>PMID:31636255</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qdj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Arnese R]]
[[Category: Clausen T]]
[[Category: Meinhart A]]